Structure of PDB 3nyt Chain A

Receptor sequence
>3nytA (length=359) Species: 208964 (Pseudomonas aeruginosa PAO1) [Search protein sequence]
MIEFIDLKNQQARIKDKIDAGIQRVLRHGQYILGPEVTELEDRLADFVGA
KYCISCANGTDALQIVQMALGVGPGDEVITPGFTYVATAETVALLGAKPV
YVDIDPRTYNLDPQLLEAAITPRTKAIIPVSLYGQCADFDAINAIASKYG
IPVIEDAAQSFGASYKGKRSCNLSTVACTSFFPSAPLGCYGDGGAIFTND
DELATAIRQIARHGQDRRYHHIRVGVNSRLDTLQAAILLPKLEIFEEEIA
LRQKVAAEYDLSLKQVGIGTPFIEVNNISVYAQYTVRMDNRESVQASLKA
AGVPTAVHYPIPLNKQPAVADEKAKLPVGDKAATQVMSLPMHPYLDTASI
KIICAALTN
3D structure
PDB3nyt Structural investigation on WlaRG from Campylobacter jejuni: A sugar aminotransferase.
ChainA
Resolution1.301 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y85 D156 Q159 F182 A185 Y219 R229
Catalytic site (residue number reindexed from 1) Y85 D156 Q159 F182 A185 Y219 R229
Enzyme Commision number 2.6.1.98: UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ULP A I5 L7 N58 G59 T60 Y85 A87 D156 A158 Q159 S180 F182 S184 H308 Y309 I5 L7 N58 G59 T60 Y85 A87 D156 A158 Q159 S180 F182 S184 H308 Y309
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0000271 polysaccharide biosynthetic process
GO:0006065 UDP-glucuronate biosynthetic process
GO:0009103 lipopolysaccharide biosynthetic process
GO:0009243 O antigen biosynthetic process
GO:0071555 cell wall organization

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3nyt, PDBe:3nyt, PDBj:3nyt
PDBsum3nyt
PubMed28028852
UniProtQ9HZ76|WBPE_PSEAE UDP-2-acetamido-2-deoxy-3-oxo-D-glucuronate aminotransferase (Gene Name=wbpE)

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